8J0N: Human EMC
cryo-EM structure of human EMC. Determined by electron microscopy at 3.47 Å resolution. Released 3 Apr 2024.
- Method
- Electron microscopy
- Resolution
- 3.47 Å
- Organism
- Homo sapiens
- Chains
- 9
- Atoms
- 18,475
- Mol. weight
- 297.44 kDa
- Released
- 3 Apr 2024
Explore 8J0N in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
8J0N contains 71 α-helices and 100 β-strands across 9 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
Chain A: 9 helices, 68 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 32-35 | 4 | 1 |
| β-strand | 40-44 | 5 | 2 |
| β-strand | 53-58 | 6 | 2 |
| β-strand | 62-67 | 6 | 2 |
| β-strand | 77-78 | 2 | 2 |
| β-strand | 90-92 | 3 | 3 |
| β-strand | 96-100 | 5 | 3 |
| β-strand | 106-111 | 6 | 3 |
| β-strand | 117-122 | 6 | 3 |
| β-strand | 130-135 | 6 | 4 |
| β-strand | 140-146 | 7 | 4 |
| β-strand | 150-155 | 6 | 4 |
| β-strand | 161-166 | 6 | 4 |
| β-strand | 175 | 1 | 5 |
| β-strand | 179-180 | 2 | 5 |
| β-strand | 185-191 | 7 | 5 |
| β-strand | 196-203 | 8 | 5 |
| β-strand | 209-216 | 8 | 5 |
| β-strand | 228-230 | 3 | 6 |
| β-strand | 234-239 | 6 | 6 |
| β-strand | 244-249 | 6 | 6 |
| β-strand | 256-260 | 5 | 6 |
| β-strand | 275-278 | 4 | 7 |
| β-strand | 290-294 | 5 | 7 |
| β-strand | 301-305 | 5 | 7 |
| β-strand | 310-315 | 6 | 7 |
| β-strand | 321-326 | 6 | 8 |
| β-strand | 331-337 | 7 | 8 |
| β-strand | 356-358 | 3 | 9 |
| β-strand | 363-365 | 3 | 9 |
| β-strand | 372-379 | 8 | 8 |
| β-strand | 385 | 1 | 8 |
| β-strand | 391-394 | 4 | 8 |
| β-strand | 405-412 | 8 | 10 |
| β-strand | 416-424 | 9 | 10 |
| α-helix | 425 | 1 | |
| β-strand | 430-433 | 4 | 10 |
| β-strand | 441-445 | 5 | 10 |
| β-strand | 452-458 | 7 | 11 |
| α-helix | 464-473 | 10 | |
| α-helix | 480-509 | 30 | |
| α-helix | 521-524 | 4 | |
| β-strand | 535-540 | 6 | 11 |
| β-strand | 544-549 | 6 | 11 |
| β-strand | 555-560 | 6 | 11 |
| β-strand | 569-574 | 6 | 12 |
| β-strand | 587-592 | 6 | 12 |
| β-strand | 599-604 | 6 | 12 |
| α-helix | 610-612 | 3 | |
| α-helix | 622-623 | 2 | |
| β-strand | 625-633 | 9 | 13 |
| β-strand | 637-643 | 7 | 13 |
| β-strand | 649-651 | 3 | 13 |
| α-helix | 656-665 | 10 | |
| β-strand | 670-674 | 5 | 14 |
| β-strand | 680-686 | 7 | 14 |
| β-strand | 692-699 | 8 | 14 |
| β-strand | 705-711 | 7 | 15 |
| β-strand | 723-725 | 3 | 16 |
| β-strand | 731-733 | 3 | 16 |
| β-strand | 734 | 1 | 17 |
| β-strand | 741-747 | 7 | 15 |
| β-strand | 757-762 | 6 | 15 |
| β-strand | 769-775 | 7 | 15 |
| β-strand | 778-786 | 9 | 17 |
| β-strand | 790-797 | 8 | 17 |
| β-strand | 802-811 | 10 | 17 |
| β-strand | 821-822 | 2 | 18 |
| β-strand | 832-839 | 8 | 17 |
| β-strand | 847-849 | 3 | 19 |
| β-strand | 860-864 | 5 | 19 |
| β-strand | 870-874 | 5 | 19 |
| α-helix | 888-893 | 6 | |
| β-strand | 919-926 | 8 | 1 |
| β-strand | 933-939 | 7 | 1 |
| β-strand | 941-947 | 7 | 1 |
| α-helix | 962-992 | 31 | |
Chain B: 16 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-8 | 6 | |
| α-helix | 12-25 | 14 | |
| α-helix | 30-43 | 14 | |
| α-helix | 49-66 | 18 | |
| α-helix | 70-82 | 13 | |
| α-helix | 87-100 | 14 | |
| α-helix | 103-116 | 14 | |
| α-helix | 121-134 | 14 | |
| α-helix | 137-151 | 15 | |
| α-helix | 155-167 | 13 | |
| α-helix | 171-184 | 14 | |
| α-helix | 189-202 | 14 | |
| α-helix | 205-222 | 18 | |
| α-helix | 227-241 | 15 | |
| α-helix | 247-269 | 23 | |
| α-helix | 278-296 | 19 | |
Chain C: 14 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-9 | 3 | |
| α-helix | 13-38 | 26 | |
| α-helix | 46-63 | 18 | |
| α-helix | 70-81 | 12 | |
| α-helix | 87-90 | 4 | |
| α-helix | 118-131 | 14 | |
| β-strand | 138-139 | 2 | 20 |
| α-helix | 146-148 | 3 | |
| α-helix | 149-152 | 4 | |
| β-strand | 165-166 | 2 | 20 |
| α-helix | 168-178 | 11 | |
| α-helix | 180-186 | 7 | |
| α-helix | 194-208 | 15 | |
| α-helix | 214-227 | 14 | |
| α-helix | 238-241 | 4 | |
| α-helix | 247-256 | 10 | |
Chain D: 9 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 13-15 | 3 | |
| α-helix | 62-72 | 11 | |
| α-helix | 75-78 | 4 | |
| α-helix | 81-90 | 10 | |
| α-helix | 96-112 | 17 | |
| α-helix | 116-123 | 8 | |
| α-helix | 127-154 | 28 | |
| α-helix | 161-165 | 5 | |
| α-helix | 168-171 | 4 | |
| β-strand | 172-173 | 2 | 18 |
| β-strand | 177-180 | 4 | 14 |
Chain E: 5 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-33 | 31 | |
| α-helix | 40-42 | 3 | |
| α-helix | 43-63 | 21 | |
| α-helix | 81-85 | 5 | |
| α-helix | 96-100 | 5 | |
Chain F: 5 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 16-44 | 29 | |
| α-helix | 48-70 | 23 | |
| α-helix | 74-77 | 4 | |
| α-helix | 82-85 | 4 | |
| α-helix | 91-107 | 17 | |
Chain G: 1 helix, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 45-52 | 8 | 21 |
| α-helix | 58-62 | 5 | |
| β-strand | 66-68 | 3 | 22 |
| β-strand | 75-77 | 3 | 22 |
| β-strand | 78 | 1 | 21 |
| β-strand | 79 | 1 | 3 |
| β-strand | 84-89 | 6 | 21 |
| β-strand | 92-96 | 5 | 23 |
| β-strand | 97-99 | 3 | 22 |
| β-strand | 108-112 | 5 | 23 |
| β-strand | 118-122 | 5 | 23 |
| β-strand | 134 | 1 | 23 |
| β-strand | 138-141 | 4 | 21 |
Chain H: 7 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-6 | 4 | 24 |
| α-helix | 8-20 | 13 | |
| β-strand | 25-32 | 8 | 24 |
| β-strand | 51-63 | 13 | 24 |
| α-helix | 68-82 | 15 | |
| β-strand | 88-95 | 8 | 24 |
| α-helix | 106-118 | 13 | |
| β-strand | 123-127 | 5 | 24 |
| α-helix | 128 | 1 | |
| β-strand | 141-146 | 6 | 24 |
| β-strand | 152-154 | 3 | 24 |
| α-helix | 164-176 | 13 | |
| α-helix | 186-191 | 6 | |
| α-helix | 200-209 | 10 | |
1 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| ER membrane protein complex subunit 1 | A | protein | 993 | Homo sapiens | Q8N766 (AlphaFold model) |
| ER membrane protein complex subunit 2 | B | protein | 297 | Homo sapiens | Q15006 (AlphaFold model) |
| ER membrane protein complex subunit 3 | C | protein | 261 | Homo sapiens | Q9P0I2 (AlphaFold model) |
| ER membrane protein complex subunit 4 | D | protein | 183 | Homo sapiens | Q5J8M3 (AlphaFold model) |
| ER membrane protein complex subunit 5 | E | protein | 131 | Homo sapiens | Q8N4V1 |
| ER membrane protein complex subunit 6 | F | protein | 110 | Homo sapiens | Q9BV81 |
| ER membrane protein complex subunit 7 | G | protein | 242 | Homo sapiens | Q9NPA0 |
| ER membrane protein complex subunit 8 | H | protein | 210 | Homo sapiens | O43402 |
| ER membrane protein complex subunit 10 | J | protein | 207 | Homo sapiens | Q5UCC4 |
Sequence of entity 1 (A), FASTA
>8J0N_1 ER membrane protein complex subunit 1 (chains A)
MAAEWASRFWLWATLLIPAAAVYEDQVGKFDWRQQYVGKVKFASLEFSPGSKKLVVATEK
NVIAALNSRTGEILWRHVDKGTAEGAVDAMLLHGQDVITVSNGGRIMRSWETNIGGLNWE
ITLDSGSFQALGLVGLQESVRYIAVLKKTTLALHHLSSGHLKWVEHLPESDSIHYQMVYS
YGSGVVWALGVVPFSHVNIVKFNVEDGEIVQQVRVSTPWLQHLSGACGVVDEAVLVCPDP
SSRSLQTLALETEWELRQIPLQSLDLEFGSGFQPRVLPTQPNPVDASRAQFFLHLSPSHY
ALLQYHYGTLSLLKNFPQTALVSFATTGEKTVAAVMACRNEVQKSSSSEDGSMGSFSEKS
SSKDSLACFNQTYTINLYLVETGRRLLDTTITFSLEQSGTRPERLYIQVFLKKDDSVGYR
ALVQTEDHLLLFLQQLAGKVVLWSREESLAEVVCLEMVDLPLTGAQAELEGEFGKKADGL
LGMFLKRLSSQLILLQAWTSHLWKMFYDARKPRSQIKNEINIDTLARDEFNLQKMMVMVT
ASGKLFGIESSSGTILWKQYLPNVKPDSSFKLMVQRTTAHFPHPPQCTLLVKDKESGMSS
LYVFNPIFGKWSQVAPPVLKRPILQSLLLPVMDQDYAKVLLLIDDEYKVTAFPATRNVLR
QLHELAPSIFFYLVDAEQGRLCGYRLRKDLTTELSWELTIPPEVQRIVKVKGKRSSEHVH
SQGRVMGDRSVLYKSLNPNLLAVVTESTDAHHERTFIGIFLIDGVTGRIIHSSVQKKAKG
PVHIVHSENWVVYQYWNTKARRNEFTVLELYEGTEQYNATAFSSLDRPQLPQVLQQSYIF
PSSISAMEATITERGITSRHLLIGLPSGAILSLPKALLDPRRPEIPTEQSREENLIPYSP
DVQIHAERFINYNQTVSRMRGIYTAPSGLESTCLVVAYGLDIYQTRVYPSKQFDVLKDDY
DYVLISSVLFGLVFATMITKRLAQVKLLNRAWR
Sequence of entity 2 (B), FASTA
>8J0N_2 ER membrane protein complex subunit 2 (chains B)
MAKVSELYDVTWEEMRDKMRKWREENSRNSEQIVEVGEELINEYASKLGDDIWIIYEQVM
IAALDYGRDDLALFCLQELRRQFPGSHRVKRLTGMRFEAMERYDDAIQLYDRILQEDPTN
TAARKRKIAIRKAQGKNVEAIRELNEYLEQFVGDQEAWHELAELYINEHDYAKAAFCLEE
LMMTNPHNHLYCQQYAEVKYTQGGLENLELSRKYFAQALKLNNRNMRALFGLYMSASHIA
SNPKASAKTKKDNMKYASWAASQINRAYQFAGRSKKETKYSLKAVEDMLETLQITQS
Sequence of entity 3 (C), FASTA
>8J0N_3 ER membrane protein complex subunit 3 (chains C)
MAGPELLLDSNIRLWVVLPIVIITFFVGMIRHYVSILLQSDKKLTQEQVSDSQVLIRSRV
LRENGKYIPKQSFLTRKYYFNNPEDGFFKKTKRKVVPPSPMTDPTMLTDMMKGNVTNVLP
MILIGGWINMTFSGFVTTKVPFPLTLRFKPMLQQGIELLTLDASWVSSASWYFLNVFGLR
SIYSLILGQDNAADQSRMMQEQMTGAAMAMPADTNKAFKTEWEALELTDHQWALDDVEEE
LMAKDLHFEGMFKKELQTSIF
Sequence of entity 4 (D), FASTA
>8J0N_4 ER membrane protein complex subunit 4 (chains D)
MTAQGGLVANRGRRFKWAIELSGPGGGSRGRSDRGSGQGDSLYPVGYLDKQVPDTSVQET
DRILVEKRCWDIALGPLKQIPMNLFIMYMAGNTISIFPTMMVCMMAWRPIQALMAISATF
KMLESSSQKFLQGLVYLIGNLMGLALAVYKCQSMGLLPTHASDWLAFIEPPERMEFSGGG
LLL
Sequence of entity 5 (E), FASTA
>8J0N_5 ER membrane protein complex subunit 5 (chains E)
MAPSLWKGLVGIGLFALAHAAFSAAQHRSYMRLTEKEDESLPIDIVLQTLLAFAVTCYGI
VHIAGEFKDMDATSELKNKTFDTLRNHPSFYVFNHRGRVLFRPSDTANSSNQDALSSNTS
LKLRKLESLRR
Sequence of entity 6 (F), FASTA
>8J0N_6 ER membrane protein complex subunit 6 (chains F)
MAAVVAKREGPPFISEAAVRGNAAVLDYCRTSVSALSGATAGILGLTGLYGFIFYLLASV
LLSLLLILKAGRRWNKYFKSRRPLFTGGLIGGLFTYVLFWTFLYGMVHVY
Sequence of entity 7 (G), FASTA
>8J0N_7 ER membrane protein complex subunit 7 (chains G)
MAAALWGFFPVLLLLLLSGDVQSSEVPGAAAEGSGGSGVGIGDRFKIEGRAVVPGVKPQD
WISAARVLVDGEEHVGFLKTDGSFVVHDIPSGSYVVEVVSPAYRFDPVRVDITSKGKMRA
RYVNYIKTSEVVRLPYPLQMKSSGPPSYFIKRESWGWTDFLMNPMVMMMVLPLLIFVLLP
KVVNTSDPDMRREMEQSMNMLNSNHELPDVSEFMTRLFSSKSSGKSSSGSSKTGKSGAGK
RR
Sequence of entity 8 (H), FASTA
>8J0N_8 ER membrane protein complex subunit 8 (chains H)
MPGVKLTTQAYCKMVLHGAKYPHCAVNGLLVAEKQKPRKEHLPLGGPGAHHTLFVDCIPL
FHGTLALAPMLEVALTLIDSWCKDHSYVIAGYYQANERVKDASPNQVAEKVASRIAEGFS
DTALIMVDNTKFTMDCVAPTIHVYEHHENRWRCRDPHHDYCEDWPEAQRISASLLDSRSY
ETLVDFDNHLDDIRNDWTNPEINKAVLHLC
Sequence of entity 9 (J), FASTA
>8J0N_9 ER membrane protein complex subunit 10 (chains J)
MAAASAGATRLLLLLLMAVAAPSRARGSGCRAGTGARGAGAEGREGEACGTVGLLLEHSF
EIDDSANFRKRGSLLWNQQDGTLSLSQRQLSEEERGRLRDVAALNGLYRVRIPRRPGALD
GLEAGGYVSSFVPACSLVESHLSDQLTLHVDVAGNVVGVSVVTHPGGCRGHEVEDVDLEL
FNTSVQLQPPTTAPGPETAAFIERLEM
Primary citation
Structural insights into human EMC and its interaction with VDAC. Li, M., Zhang, C., Xu, Y. et al. Aging (Albany NY) (2024) 16:5501-5525. DOI 10.18632/aging.205660 · PubMed
Other PDB entries of the same protein (UniProt Q8N766 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 8J0O 3.32 Å, cryo-EM structure of human EMC and VDAC
- 7ADO 3.39 Å, Cryo-EM structure of human ER membrane protein complex in lipid nanodiscs
- 6WW7 3.4 Å, Structure of the human ER membrane protein complex in a lipid nanodisc
- 8EOI 3.4 Å, Structure of a human EMC:human Cav1.2 channel complex in GDN detergent
- 7ADP 3.6 Å, Cryo-EM structure of human ER membrane protein complex in GDN detergent
- 8S9S 3.6 Å, Structure of the human ER membrane protein complex (EMC) in GDN
- 9ZZ6 4.16 Å, The ER membrane protein complex acts as a chaperone to promote voltage-gated calcium…
- 6Z3W 6.4 Å, Human ER membrane protein complex
- 9C7V 6.6 Å, Structure of the human BOS:human EMC complex in GDN
Browse structure collections
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